ArticlePloS one2013
Structure-function-immunogenicity studies of PfEMP1 domain DBL2βPF11_0521, a malaria parasite ligand for ICAM-1.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Malaria Parasite Plasmodium falciparum Proteins on the Surface of Infected Erythrocytes as Targets for Novel Drug Discovery.Biochemistry. Biokhimiia · 2022Review
- Small Molecule Compounds Identified from Mixture-Based Library Inhibit Binding betweenInternational journal of molecular sciences · 2021Article
- Structural insights into diverse modes of ICAM-1 binding byProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sticking for a Cause: The Falciparum Malaria Parasites Cytoadherence Paradigm.Frontiers in immunology · 2019Review
- Plasmodium falciparum infected erythrocytes can bind to host receptors integrins αVβ3 and αVβ6 through DBLδ1_D4 domain of PFL2665c PfEMP1 protein.Scientific reports · 2018Article
- Antibodies to Intercellular Adhesion Molecule 1-Binding Plasmodium falciparum Erythrocyte Membrane Protein 1-DBLβ Are Biomarkers of Protective Immunity to Malaria in a Cohort of Young Children from Papua New Guinea.Infection and immunity · 2018Article
- In silico guided reconstruction and analysis of ICAM-1-binding var genes from Plasmodium falciparum.Scientific reports · 2018Article
- ICAM-1 is a key receptor mediating cytoadherence and pathology in the Plasmodium chabaudi malaria model.Malaria journal · 2017Article
- The Severity of Plasmodium falciparum Infection Is Associated with Transcript Levels ofInfection and immunity · 2017Article
- Cytoadhesion to gC1qR through Plasmodium falciparum Erythrocyte Membrane Protein 1 in Severe Malaria.PLoS pathogens · 2016Article
- Plasmodium falciparum var genes expressed in children with severe malaria encode CIDRα1 domains.EMBO molecular medicine · 2016Article
- Progress and prospects for blood-stage malaria vaccines.Expert review of vaccines · 2016Review
- High-throughput screening platform identifies small molecules that prevent sequestration of Plasmodium falciparum-infected erythrocytes.The Journal of infectious diseases · 2015Article
- An analysis of the binding characteristics of a panel of recently selected ICAM-1 binding Plasmodium falciparum patient isolates.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Plasmodium falciparum virulence has been ascribed to its ability to sequester in deep vascular beds, mediated by the variant surface antigen family PfEMP1 binding endothelial receptors like ICAM-1. We previously observed that naturally-acquired antibodies that block a PfEMP1 domain, DBL2β of PF11_0521 allele, from binding to the human ICAM1 receptor, reduce the risk of malaria hospitalization in children. Here, we find that DBL2βPF11_0521 binds ICAM-1 in the low nM range and relate the structure of this domain with its function and immunogenicity. We demonstrate that the interaction with ICAM-1 is not impaired by point mutations in the N-terminal subdomain or in the flexible Loop 4 of DBL2βPF11_0521, although both substructures were previously implicated in binding ICAM-1. These data will help to refine the existing model of DBLβ::ICAM-1 interactions. Antibodies raised against full-length DBL2βPF11_0521, but not truncated forms lacking the N terminal fragment, block its interaction with ICAM-1. Our data suggest that full length domain is optimal for displaying functional epitopes and has a broad surface of interaction with ICAM-1 that is not disrupted by individual amino acid substitutions at putative key residues. This information might be important for the future design of anti-malarial vaccines based on PfEMP1 antigens.
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